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Functional characterization of vertebrate nonmuscle myosin IIB isoforms using Dictyostelium chimeric myosin II.
| Title: | Functional characterization of vertebrate nonmuscle myosin IIB isoforms using Dictyostelium chimeric myosin II. |
| Authors: | Takahashi, M. Browse this author →KAKEN DB | | Takahashi, K. Browse this author | | Hiratsuka, Y. Browse this author | | Uchida, K. Browse this author | | Yamagishi, A. Browse this author | | Uyeda, T Q Browse this author | | Yazawa, M. Browse this author |
| Issue Date: | 12-Jan-2001 |
| Publisher: | American Society for Biochemistry and Molecular Biology |
| Journal Title: | The Journal of biological chemistry |
| Volume: | 276 |
| Issue: | 2 |
| Start Page: | 1034 |
| End Page: | 1040 |
| Publisher DOI: | 10.1074/jbc.M005370200 |
| PMID: | 11042201 |
| Abstract: | The alternatively spliced isoform of nonmuscle myosin II heavy chain B (MHC-IIB) with an insert of 21 amino acids in the actin-binding surface loop (loop 2), MHC-IIB(B2), is expressed specifically in the central nervous system of vertebrates. To examine the role of the B2 insert in the motor activity of the myosin II molecule, we expressed chimeric myosin heavy chain molecules using the Dictyostelium myosin II heavy chain as the backbone. We replaced the Dictyostelium native loop 2 with either the noninserted form of loop 2 from human MHC-IIB or the B2-inserted form of loop 2 from human MHC-IIB(B2). The transformant Dictyostelium cells expressing only the B2-inserted chimeric myosin formed unusual fruiting bodies. We then assessed the function of chimeric proteins, using an in vitro motility assay and by measuring ATPase activities and binding to F-actin. We demonstrate that the insertion of the B2 sequence reduces the motor activity of Dictyostelium myosin II, with reduction of the maximal actin-activated ATPase activity and a decrease in the affinity for actin. In addition, we demonstrate that the native loop 2 sequence of Dictyostelium myosin II is required for the regulation of the actin-activated ATPase activity by phosphorylation of the regulatory light chain. |
| Rights: | This research was originally published in Journal Name. Author(s). Title. Journal Name. Year; Vol:pp-pp. © the American Society for Biochemistry and Molecular Biology. |
| Type: | article |
| URI: | http://hdl.handle.net/2115/52172 |
| Appears in Collections: | 理学院・理学研究院 (Graduate School of Science / Faculty of Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 高橋 正行
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